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Render Timestamp: 2024-12-20T10:58:02.105Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-30 01:55:27.976
Product last modified at: 2024-12-17T18:55:06.075Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
  1. Products /
  2. Primary Antibodies /
  3. Na,K-ATPase β1 (D6U8Q) Rabbit mAb
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Na,K-ATPase β1 (D6U8Q) Rabbit mAb #44759

Filter:
  • WB

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 45-55
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Na,K-ATPase β1 (D6U8Q) Rabbit mAb recognizes endogenous levels of total Na,K-ATPase β1 protein.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro200 of human Na,K-ATPase β1 protein.

    Background

    The Na,K-ATPase is an integral membrane heterodimer belonging to the P-type ATPase family. This ion channel uses the energy derived from ATP hydrolysis to maintain membrane potential by driving sodium export and potassium import across the plasma membrane against their electrochemical gradients. It is composed of a catalytic α subunit and a β subunit (reviewed in 1). Several phosphorylation sites have been identified for the α1 subunit. Tyr10 is phosphorylated by an as yet undetermined kinase (2), Ser16 and Ser23 are phosphorylated by PKC, and Ser943 is phosphorylated by PKA (3-5). All of these sites have been implicated in the regulation of enzyme activity in response to hormones and neurotransmitters, altering trafficking and kinetic properties of Na,K-ATPase. Altered phosphorylation in response to angiotensin II stimulates activity in the rat proximal tubule (6). Na,K-ATPase is also involved in other signal transduction pathways. Insulin regulates its localization in differentiated primary human skeletal muscle cells, and this regulation is dependent on ERK1/2 phosphorylation of the α subunit (7). Na,K-ATPase and Src form a signaling receptor complex that affects regulation of Src kinase activity and, subsequently, its downstream effectors (8,9).
    Na,K-ATPase β1 is the non-catalytic subunit of Na,K-ATPase. It is required for stabilization, maturation, and translocation of the catalytic α subunit to the plasma membrane(10-12). Na,K-ATPase β1 also mediates the trans-dimerization of Na,K-ATPase between neighboring cells where it regulates the integrity of tight junctions (13-17). Glutathionylation of NA,K-ATPase β1 regulates the ion pump activity of Na,K-ATPase (18). Research studies have shown that Na,K-ATPase β1 is a target of the Sonic Hedgehog signaling pathway and may be involved in suppressing tumor development and progression (19). ATP1B1, the gene encoding Na,K-ATPase β1, is epigenetically silenced by promoter methylation in both renal cell carcinoma cell lines and patient tissues (20).
    1. Therien, A.G. and Blostein, R. (2000) Am J Physiol Cell Physiol 279, C541-66.
    2. Féraille, E. et al. (1999) Mol Biol Cell 10, 2847-59.
    3. Fisone, G. et al. (1994) J Biol Chem 269, 9368-73.
    4. Feschenko, M.S. and Sweadner, K.J. (1995) J Biol Chem 270, 14072-7.
    5. Beguin, P. et al. (1994) J Biol Chem 269, 24437-45.
    6. Yingst, D.R. et al. (2004) Am J Physiol Renal Physiol 287, F713-21.
    7. Al-Khalili, L. et al. (2004) J Biol Chem 279, 25211-8.
    8. Tian, J. et al. (2006) Mol Biol Cell 17, 317-26.
    9. Liang, M. et al. (2006) J Biol Chem 281, 19709-19.
    10. Beggah, A.T. et al. (1997) J Biol Chem 272, 10318-26.
    11. Hasler, U. et al. (1998) J Biol Chem 273, 30826-35.
    12. Rajasekaran, S.A. et al. (2004) Mol Biol Cell 15, 3224-32.
    13. Rajasekaran, S.A. et al. (2001) Mol Biol Cell 12, 3717-32.
    14. Rajasekaran, A.K. and Rajasekaran, S.A. (2003) Am J Physiol Renal Physiol 285, F388-96.
    15. Bab-Dinitz, E. et al. (2009) Biochemistry 48, 8684-91.
    16. Tokhtaeva, E. et al. (2011) J Biol Chem 286, 25801-12.
    17. Vagin, O. et al. (2012) Am J Physiol Cell Physiol 302, C1271-81.
    18. Figtree, G.A. et al. (2012) Free Radic Biol Med 53, 2263-8.
    19. Lee, S.J. et al. (2015) Mol Cancer 14, 159.
    20. Selvakumar, P. et al. (2014) Epigenetics 9, 579-86.

    Database Links

    UniProt ID: P05026


    Entrez-Gene Id: 481


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